eF-site ID 1egc-ABCD PDB Code 1egc Chain A, B, C, D click to enlarge Title STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA Classification ELECTRON TRANSFER Compound MEDIUM CHAIN ACYL-COA DEHYDROGENASE Source null (ACADM_HUMAN) Sequence A:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN B:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN C:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN D:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain A residue 255 type sequence E description CATALYTIC BASE IN CHAIN A source : CA1 2) chain B residue 255 type sequence E description CATALYTIC BASE IN CHAIN B source : CA2 3) chain C residue 255 type sequence E description CATALYTIC BASE IN CHAIN C source : CA3 4) chain D residue 255 type sequence E description CATALYTIC BASE IN CHAIN D source : CA4 5) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 6) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 7) chain A residue 141 type sequence G description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 8) chain A residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 9) chain A residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 10) chain A residue 168 type sequence T description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 11) chain A residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 12) chain A residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 13) chain A residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 14) chain A residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 15) chain A residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 16) chain A residue 256 type sequence R description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 17) chain A residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 18) chain A residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 19) chain A residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 20) chain A residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 21) chain A residue 388 type sequence R description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 22) chain B residue 284 type sequence F description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 23) chain A residue 284 type sequence F description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 24) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 25) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 26) chain B residue 136 type sequence T description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 27) chain B residue 141 type sequence G description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 28) chain B residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 29) chain B residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 30) chain B residue 145 type sequence A description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 31) chain B residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 32) chain B residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 33) chain B residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 34) chain B residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 35) chain B residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 36) chain B residue 256 type sequence R description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 37) chain B residue 259 type sequence V description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 38) chain B residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 39) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 40) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 41) chain B residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 42) chain B residue 381 type sequence I description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 43) chain C residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 44) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 45) chain B residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 46) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 47) chain C residue 99 type sequence E description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 48) chain C residue 100 type sequence G description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 49) chain C residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 50) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 51) chain C residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 52) chain C residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 53) chain C residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 54) chain C residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 55) chain C residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 56) chain C residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 57) chain C residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 58) chain C residue 259 type sequence V description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 59) chain C residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 60) chain C residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 61) chain C residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 62) chain C residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 63) chain C residue 388 type sequence R description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 64) chain D residue 95 type sequence Q description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 65) chain D residue 96 type sequence T description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 66) chain D residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 67) chain D residue 141 type sequence G description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 68) chain D residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 69) chain D residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 70) chain D residue 145 type sequence A description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 71) chain D residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 72) chain D residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 73) chain D residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 74) chain D residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 75) chain D residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 76) chain D residue 256 type sequence R description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 77) chain D residue 324 type sequence R description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 78) chain D residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 79) chain D residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 80) chain D residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 81) chain D residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 82) chain D residue 381 type sequence I description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 83) chain D residue 388 type sequence R description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 84) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 85) chain A residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 86) chain A residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 87) chain A residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 88) chain A residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 89) chain A residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 90) chain A residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 91) chain A residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 92) chain A residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 93) chain A residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 94) chain A residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 95) chain A residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 96) chain A residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 97) chain B residue 277 type sequence Y description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 98) chain B residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 99) chain B residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 100) chain B residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 101) chain B residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 102) chain B residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 103) chain B residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 104) chain B residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 105) chain B residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 106) chain D residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 107) chain A residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 108) chain A residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 109) chain A residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 110) chain A residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 111) chain A residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 112) chain A residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 113) chain A residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 114) chain A residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 115) chain A residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 116) chain B residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 117) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 118) chain B residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 119) chain B residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 120) chain B residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 121) chain B residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 122) chain B residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 123) chain B residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 124) chain B residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 125) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 126) chain B residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 127) chain B residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 128) chain C residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 129) chain B residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 130) chain C residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 131) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 132) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 133) chain C residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 134) chain C residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 135) chain C residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 136) chain C residue 167 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 137) chain C residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 138) chain C residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 139) chain C residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 140) chain C residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 141) chain C residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 142) chain C residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 143) chain D residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 144) chain D residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 145) chain D residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 146) chain D residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 147) chain D residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 148) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 149) chain D residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 150) chain D residue 352 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 151) chain D residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 152) chain A residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 153) chain C residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 154) chain C residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 155) chain C residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 156) chain C residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 157) chain C residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 158) chain C residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 159) chain C residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 160) chain C residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 161) chain C residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 162) chain D residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 163) chain D residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 164) chain D residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 165) chain D residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 166) chain D residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 167) chain D residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 168) chain D residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 169) chain D residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 170) chain D residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 171) chain D residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 172) chain D residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 173) chain D residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 174) chain A residue 349-368 type prosite sequence QILGGNGFNTEYPVEKLMRD description ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGnGFntEypveKlmrD source prosite : PS00073 175) chain A residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 176) chain B residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 177) chain C residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 178) chain D residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 179) chain A residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 180) chain B residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 181) chain B residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 182) chain C residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 183) chain C residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 184) chain D residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 185) chain D residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 186) chain A residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 187) chain A residue 133 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 188) chain A residue 166 type BINDING sequence W description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 189) chain A residue 291 type BINDING sequence H description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 190) chain B residue 133 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 191) chain D residue 291 type BINDING sequence H description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 192) chain D residue 133 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 193) chain D residue 166 type BINDING sequence W description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 194) chain C residue 291 type BINDING sequence H description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 195) chain B residue 166 type BINDING sequence W description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 196) chain B residue 291 type BINDING sequence H description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 197) chain C residue 133 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 198) chain C residue 166 type BINDING sequence W description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 199) chain A residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 200) chain D residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 201) chain D residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 202) chain D residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 203) chain D residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 204) chain A residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 205) chain C residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 206) chain C residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 207) chain C residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 208) chain B residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 209) chain B residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 210) chain B residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 211) chain B residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 212) chain C residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 213) chain A residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 214) chain A residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 215) chain B residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 216) chain B residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 217) chain C residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 218) chain C residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 219) chain C residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 220) chain C residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 221) chain C residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 222) chain D residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 223) chain D residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 224) chain D residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 225) chain D residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 226) chain D residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 227) chain A residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 228) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 229) chain A residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 230) chain A residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 231) chain B residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 232) chain B residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 233) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 234) chain A residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 235) chain B residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 236) chain A residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 237) chain C residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 238) chain D residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 239) chain C residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 240) chain C residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 241) chain D residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 242) chain D residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 243) chain A residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 244) chain A residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 245) chain B residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 246) chain B residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 247) chain A residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 248) chain B residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 249) chain C residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 250) chain D residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 251) chain A residue 134-146 type prosite sequence CVTEPGAGSDVAG description ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CVTEpgAGSDvaG source prosite : PS00072

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